Literature summary for 4.3.3.7 extracted from

Rice, E.A.; Bannon, G.A.; Glenn, K.C.; Jeong, S.S.; Sturman, E.J.; Rydel, T.J.
Characterization and crystal structure of lysine insensitive Corynebacterium glutamicum dihydrodipicolinate synthase (cDHDPS) protein (2008), Arch. Biochem. Biophys., 480, 111-121.

Search for more literature for 4.3.3.7

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli STBL2, pET23b vector	Corynebacterium glutamicum

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop method, data collection and refinement statistics, refinement resolution originally extended to 3.0 A, gradually increased to 2.5 A, and finally to 2.2 A, structural similarities to other dihydrodipicolinate synthase	Corynebacterium glutamicum

Inhibitors

Inhibitors	Comment	Organism	Structure
3-Bromopyruvate	competitive inhibition, pyruvate as varied substrate	Corynebacterium glutamicum
L-aspartate	competitive inhibition, L-aspartate 4-semialdehyde as varied substrate	Corynebacterium glutamicum
L-aspartate 4-semialdehyde	uncompetitive inhibition by high concentrations of, no overcome by increasing pyruvate concentrations from 5 to 15 mM	Corynebacterium glutamicum
L-lysine	lack of feedback inhibition, not regulated under normal physiological conditions	Corynebacterium glutamicum
oxaloacetate	non-competitive inhibition, pyruvate as varied substrate	Corynebacterium glutamicum
Succinic semialdehyde	uncompetitive inhibition, L-aspartate 4-semialdehyde as varied substrate	Corynebacterium glutamicum

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.32	-	pyruvate	2.5 mM pyruvate replaced by 0.1-2 mM, no substrate inhibition observed at high concentrations of pyruvate	Corynebacterium glutamicum
0.63	-	L-aspartate 4-semialdehyde	reaction mixture includes 100 mM Tris-HCl, 2.5 mM pyruvate, 0.05-0.1 microg dihydrodipicolinate synthase and 0.2 mM NADPH, from 5.6 to 22.4 mM plots deviate from typical Michaelis-Menten kinetics, increased concentration fits an uncompetitive substrate inhibition model	Corynebacterium glutamicum

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
73000	-	approximating the size of two DHDPS proteins interacting to form a dimer	Corynebacterium glutamicum
158000	-	native protein, gel filtration, homotetramer predicted	Corynebacterium glutamicum

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium glutamicum	P19808	-	-

Purification (Commentary)

Purification (Comment)	Organism
gel filtration, SDS-PAGE	Corynebacterium glutamicum

Source Tissue

Source Tissue	Comment	Organism	Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	structure in vicinity of the putative binding site for S-lysine indicates that the allosteric binding site in the Escherichia coli dihydrodipicolinate synthase does not exist in the enzyme of Corynebacterium glutamicum, difference of three non-conservative amino acids substitutions, explains lack of feedback inhibition by lysine in Corynebacterium glutamicum	Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-aspartate 4-semialdehyde + pyruvate	lysine insensitivity of dihydrodipicolinate synthase analyzed, catalytic lysine residue forms a Schiff base adduct with pyruvate, active site lysine residues (K176a, K176b)	Corynebacterium glutamicum	dihydrodipicolinate + H2O	-	?

Subunits

Subunits	Comment	Organism
homotetramer	ribbons rendition of homotetramer in the crystal lattice shown	Corynebacterium glutamicum

Synonyms

Synonyms	Comment	Organism
cDHDPS	-	Corynebacterium glutamicum

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
213	-	L-aspartate 4-semialdehyde	-	Corynebacterium glutamicum

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
660	-	5 mM pyruvate, addition of 0-716 mM lysine, lack of feedback inhibition	Corynebacterium glutamicum	L-lysine

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Release 2023.1 (January 2023)